Information on EC 1.3.3.6 - acyl-CoA oxidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.3.3.6
-
RECOMMENDED NAME
GeneOntology No.
acyl-CoA oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(4Z,7Z,10Z,13Z,16Z)-docosa-4,7,10,13,16-pentaenoate biosynthesis (6-desaturase)
-
-
10-cis-heptadecenoyl-CoA degradation (yeast)
-
-
10-trans-heptadecenoyl-CoA degradation (reductase-dependent, yeast)
-
-
6-gingerol analog biosynthesis (engineered)
-
-
9-cis, 11-trans-octadecadienoyl-CoA degradation (isomerase-dependent, yeast)
-
-
alpha-Linolenic acid metabolism
-
-
Biosynthesis of secondary metabolites
-
-
Biosynthesis of unsaturated fatty acids
-
-
docosahexaenoate biosynthesis III (6-desaturase, mammals)
-
-
fatty acid beta-oxidation (peroxisome, yeast)
-
-
fatty acid beta-oxidation II (peroxisome)
-
-
fatty acid beta-oxidation V (unsaturated, odd number, di-isomerase-dependent)
-
-
fatty acid beta-oxidation VI (peroxisome)
-
-
Fatty acid degradation
-
-
jasmonic acid biosynthesis
-
-
lipid metabolism
-
-
Metabolic pathways
-
-
methyl ketone biosynthesis (engineered)
-
-
oleate beta-oxidation (isomerase-dependent, yeast)
-
-
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:oxygen 2-oxidoreductase
A flavoprotein (FAD). Acts on CoA derivatives of fatty acids with chain lengths from 8 to 18.
CAS REGISTRY NUMBER
COMMENTARY hide
61116-22-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
six ACX genes, acx1-acx6. ACX6 is not expressed
-
-
Manually annotated by BRENDA team
Arthrobacter nicotianae
inducible
-
-
Manually annotated by BRENDA team
strain 2-4-1
SwissProt
Manually annotated by BRENDA team
Arthrobacter sp. 02.04.2001
strain 2-4-1
SwissProt
Manually annotated by BRENDA team
Arthrobacter ureafaciens
strain NBRC 12140
SwissProt
Manually annotated by BRENDA team
Arthrobacter ureafaciens NBRC 12140
strain NBRC 12140
SwissProt
Manually annotated by BRENDA team
gene aoxA
-
-
Manually annotated by BRENDA team
strain GHA
-
-
Manually annotated by BRENDA team
strain GHA
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Candida sp.
-
-
-
Manually annotated by BRENDA team
pK 233, inducible by growth on alkanes
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cucumber
-
-
Manually annotated by BRENDA team
Cucurbita sp.
pumpkin
-
-
Manually annotated by BRENDA team
soybean
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
no activity in Sporidiobolus pararoseus
strain CBS484
-
-
Manually annotated by BRENDA team
no activity in Sporidiobolus pararoseus CBS484
strain CBS484
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
spinach
-
-
Manually annotated by BRENDA team
Sporidiobolus ruineniae
strain CBS5001
-
-
Manually annotated by BRENDA team
Sporidiobolus ruineniae CBS5001
strain CBS5001
-
-
Manually annotated by BRENDA team
from Lophius americanus
-
-
Manually annotated by BRENDA team
mung bean
-
-
Manually annotated by BRENDA team
medium-chain specific isoform, MCOX, and short-chain specific isoform, SCOX
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
-
adult peroxisomal acyl-coenzyme A oxidase deficiency, formerly also called pseudoneonatal adrenoleucodystrophy, is a disorder of peroxisomal fatty acid oxidation with a severe presentation with cerebellar and brainstem atrophy, phenotype, overview. Accumulation of very-long-chain fatty acids is the only diagnostic marker for SCOX deficiency
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,16-hexadecadioyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
16-hydroxy-palmitoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
2-oxoheptadecyldethio-CoA + O2
?
show the reaction diagram
-
-
-
-
?
4,8,12-trimethyl-tridecanoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
4-methyl-nonanoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
6-phenyl-6-phenyl-hexanoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
acyl-CoA + O2
trans-2-enoyl-CoA + H2O2
show the reaction diagram
-
assay at 25C
-
-
ir
arachidoyl-CoA + O2
2-trans-eicosenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
behenoyl-CoA + O2
2-trans-docosenoyl-CoA + H2O2
show the reaction diagram
butyryl-CoA + O2
trans-2-butenoyl-CoA + H2O2
show the reaction diagram
cis-3-decenoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
cis-3-hexenoyl-CoA + O2
?
show the reaction diagram
-
best substrate for the isomerase activity of the enzyme
-
-
?
cis-3-octenoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
dec-4-cis-enoyl-CoA + O2
2-trans-4-cis-decadienoyl-CoA + H2O2
show the reaction diagram
dec-4-trans-enoyl-CoA + O2
2-trans-4-trans-decadienoyl-CoA + H2O2
show the reaction diagram
-
-
-
?
decanoyl-CoA + O2
trans-2-decenoyl-CoA + H2O2
show the reaction diagram
dicarboxylic acid-CoAs with 6-16 carbon atoms + O2
?
show the reaction diagram
-
-
-
-
?
dodecanoyl-CoA + O2
(2E)-dodec-2-enoyl-CoA + H2O2
show the reaction diagram
eicosapentaenoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
furylpropionyl-CoA + O2
furylacryloyl-CoA + H2O2
show the reaction diagram
-
also oxidizes aromatic/heterocyclic ring-substituted chromogenic substrates
-
?
hexadecanedioyl-CoA + O2
?
show the reaction diagram
hexanoyl-CoA + O2
(2E)-hex-2-enoyl-CoA + H2O2
show the reaction diagram
indole-3-butyric acid-CoA + O2
?
show the reaction diagram
-
-
-
-
?
jasmonic acid-CoA + O2
?
show the reaction diagram
preferred substrate of ACX1
-
-
?
lauroyl-CoA + O2
trans-2-dodecenoyl-CoA + H2O2
show the reaction diagram
leuko-dichlorofluorescein + O2
?
show the reaction diagram
-
-
-
-
?
lignoceroyl-CoA + O2
?
show the reaction diagram
linoleoyl-CoA + O2
2-trans-9-trans-12-trans-octadecatrienoyl-CoA + H2O2
show the reaction diagram
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
show the reaction diagram
nonanoyl-CoA + O2
trans-2-nonenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
octadecanoyl-CoA + O2
?
show the reaction diagram
preferred substrate of ACX2
-
-
?
octanoyl-CoA + O2
trans-2-octenoyl-CoA + H2O2
show the reaction diagram
oleoyl-CoA + O2
2-trans-9-trans-octadecendienoyl-CoA + H2O2
show the reaction diagram
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
show the reaction diagram
palmitoyl-CoA + O2
trans-2,3-dehydropalmitoyl-CoA
show the reaction diagram
stearoyl-CoA + O2
trans-2-octadecenoyl-CoA + H2O2
show the reaction diagram
trans-3-decenoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
trans-3-hexenoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
trans-3-octenoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
trihydroxycoprostanoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
palmitoyl-CoA + O2
trans-2,3-dehydropalmitoyl-CoA
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-bromopalmitic acid
-
-
2-Bromopalmitoyl-CoA
-
-
2-tetradecylglycidic acid
-
-
3,4-pentadienoyl-CoA
-
rapid, irreversible
3-ketoacyl-CoA substrate analogues
-
complex formation with anionic forms of 3-ketoacyl-CoA
3-ketohexadecanoyl-CoA
-
-
3-octynoyl-CoA
-
irreversible
5,5'-dithiobis(2-nitro-benzoic acid)
-
inactivates by modification of sulfhydryl groups and loss of FAD
acetyl-CoA
-
competitive inhibition
antimycin A
C16-C18 fatty acyl-CoA
-
at fairly low concentrations
Detergents
FMN
-
uncompetitive inhibition
indole-3-butyric acid
-
inhibits root elongation
Mercuric acetate
-
-
N-ethylmaleimide
oct-2-en-4-ynoyl-CoA
-
irreversible inactivation, pH dependent, higher under basic condition
p-chloromercuribenzoate
Phenol
-
high concentration, magnitude of inhibition depends on the nature of the acyl-CoA substrate
Phenylmethylsulfonylfluoride
Arthrobacter nicotianae
-
slight inhibition
additional information
-
glutathione protects against inhibition with sulfhydryl reagents
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-Amino-1,2,4-triazole
-
enhances acyl-CoA oxidation, avoids H2O2 consumption by endogenous catalase
alpha-linolenic acid-rich perilla oil
-
stimulates
-
bovine serum albumin
-
slightly increases ACO activity, maximum value of ACO acitvity at 0.036 mM
-
casein
stimulates
di-(2-ethylhexyl)phthalate
-
-
fish oil
-
markedly increases enzyme activity
-
growth hormone
-
increases the mRNA of acyl CoA oxidase, directly induces the expression of AOX in adipocytes through STAT5A binding to the -1841 to -1825 site within the AOX promoter
-
jasmonate
upregulates expression of ACX1, starts 4 h after treatment and remains elevated until 24 h
leptin
-
3fold increased activity at 100 ng/ml acute treatment
-
MnCl2
Arthrobacter nicotianae
-
slightly activating
n-Alkane
-
increases ACO activity progressively with palmitoyl-CoA by 23%, with stearoyl-CoA by 42%, with behenoyl-CoA by 47% and with lignoceroyl-CoA by 75%
-
perfluorooctane sulfonate
perilla oil
-
elevates AOX activity in a 4-day fedding, the effect is gradually decreased in a 4-week feeding
-
Peroxidase
-
stimulates, maximum value of ACO acitvity at 0.24 mg
-
Phenol
-
low concentration, magnitude of activation depends on the nature of the acyl-CoA substrate
prolactin
-
increases the mRNA of acyl CoA oxidase
-
Propionate
-
increase in propionate concentration lead to increase of enzyme amount
tetracosane
-
stimulates, highest activity with lignoceroyl-CoA as substrate
Triton X-100
-
stimulates, maximum value of ACO acitvity at 0.08%
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0335
arachidoyl-CoA
-
-
0.032 - 0.1319
Butyryl-CoA
0.044 - 0.054
cis-3-decenoyl-CoA
0.063 - 0.076
cis-3-hexenoyl-CoA
0.054 - 0.057
cis-3-Octenoyl-CoA
0.0093
Dec-4-cis-enoyl-CoA
-
-
0.002 - 0.024
decanoyl-CoA
0.0157 - 0.1
Dodecanoyl-CoA
0.00633
Hexadecanedioyl-CoA
30C
0.006 - 0.092
Hexanoyl-CoA
0.013 - 0.027
Lauroyl-CoA
0.0025
lignoceroyl-CoA
-
-
0.0073 - 0.019
linoleoyl-CoA
0.0053 - 0.029
myristoyl-CoA
0.005
O2
-
-
0.042 - 0.087
Octanoyl-CoA
0.011 - 0.046
oleoyl-CoA
0.00000002 - 0.09
palmitoyl-CoA
0.0044 - 0.034
stearoyl-CoA
0.018
tetradecanoyl-CoA
30C
0.056 - 0.064
trans-3-decenoyl-CoA
0.063 - 0.083
trans-3-hexenoyl-CoA
0.059 - 0.066
trans-3-octenoyl-CoA
additional information
additional information
-
overview: Km of several monocarboxylic and dicarboxylic acyl-CoA as substrates
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.225
Butyryl-CoA
Arthrobacter nicotianae
-
-
0.04 - 0.06167
cis-3-decenoyl-CoA
0.165 - 0.35
cis-3-hexenoyl-CoA
0.053 - 0.075
cis-3-Octenoyl-CoA
1.53
decanoyl-CoA
Yarrowia lipolytica
-
recombinant enzyme
0.089 - 8.59
Hexanoyl-CoA
0.07 - 3.47
Octanoyl-CoA
78
palmitoyl-CoA
Arthrobacter ureafaciens
Q33DR0
-
0.0053 - 0.01567
trans-3-decenoyl-CoA
0.0283 - 0.05
trans-3-hexenoyl-CoA
0.012 - 0.045
trans-3-octenoyl-CoA
additional information
additional information
Candida tropicalis
-
pH-dependency of turnover number
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00047
3-ketohexadecanoyl-CoA
-
-
0.3
acetyl-CoA
-
-
0.03 - 0.32
CoA
0.55
FMN
-
-
0.045
oct-2-en-4-ynoyl-CoA
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000016
-
activity in one peroxisomal acyl-coenzyme A oxidase deficiency patient, pH not specified in the publication, temperature not specified in the publication
0.0006
-
liver homogenate
0.00502
-
glucose-grown cultures with stearoyl-CoA as substrate
0.00571
-
glucose-grown cultures with behenoyl-CoA as substrate
0.00613
-
glucose-grown cultures with palmitoyl-CoA as substrate
0.00615
-
glucose-grown cultures with lignoceroyl-CoA as substrate
0.00714
-
alkane-grown cultures with stearoyl-CoA as substrate
0.00758
-
alkane-grown cultures with palmitoyl-CoA as substrate
0.008 - 4
-
alkane-grown cultures with behenoyl-CoA as substrate
0.0108
-
alkane-grown cultures with lignoceroyl-CoA as substrate
0.375
-
purified isozyme SCOX
1.7
Arthrobacter ureafaciens
crude enzyme; crude extract, at 37C
1.95
-
recombinant enzyme, purified
2.04
-
purified enzyme
2.12
-
purified enzyme
5.3
-
highly purified isozyme MCOX
27
-
purified enzyme
27.2
-
purified enzyme
58
-
purified enzyme
60.9
Arthrobacter ureafaciens
purified enzyme; purified recombinant enzyme, at 37C
77.14
Arthrobacter nicotianae
-
purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
recombinant enzyme
7.5
Arthrobacter ureafaciens
-
7.5 - 8.5
-
optimal palmitoyl-CoA oxidase activity for ACOX1b
8.3 - 8.5
-
-
8.3 - 8.6
-
isozyme SCOX
8.5
-
optimal palmitoyl-CoA oxidase activity for ACOX1a
8.6
-
isozyme MCOX
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10
-
pH 7: about 30% of activity maximum, pH 10: about 5% of activity maximum, inactive below pH 6.5
7.2 - 9.3
-
both isoforms
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28 - 38
-
recombinant enzyme
37.5
-
the ACOX1b isoform has a maximum specific activity around 37.5C
40
-
the maximum specific activity for ACOX1a is obtained at 40C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 55
-
recombinant enzyme, at 5C, 21% activity, at 55C, 78% activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
low content
Manually annotated by BRENDA team
-
before anthesis
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
posterior
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
-
SDS-PAGE
60000
-
isoform SCOX, gel filtration
62000
-
isoform MCOX, gel filtration
72000
-
Western blot analysis
76400
predicted
76500
Arthrobacter ureafaciens
predicted from amino acid sequence
81000
-
isoform ACOX1a and ACOX1b, SDS-PAGE
100000
Arthrobacter nicotianae
-
gel filtration
136000
-
gel filtration
139000
140000
-
native AtACX1 and AtACX2, and recombinant AtACX1, gel filtration
145000
-
inducible fatty acyl-CoA oxidase, gel filtration
150000
160000
Arthrobacter ureafaciens
native-PAGE
180000
Arthrobacter ureafaciens
SDS-PAGE, recombinant enzyme
190000
Arthrobacter ureafaciens
gel filtration; gel filtration, recombinant enzyme
427000
-
noninducible fatty acyl-CoA oxidase, gel filtration
552000
-
ultracentrifugation
600000
-
sedimentation equilibrium
660000
-
recombinant AtACX2, aggregation in E. coli, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
-
6 * 69000, liver, SDS-PAGE, noninducible trihydroxyprostanoyl-CoA oxidase
homodimer
homotetramer
4 * 47000, ACX4
monomer
-
1 * 62000, isoform MCOX, SDS-PAGE
octamer
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by the hanging drop vapor diffusion technique, ACX4-acetoacetyl-CoA crystals to 2.7 A resolution, of His-tagged ACX4 to 3.9 A resolution
-
hanging-drop vapor-diffusion method, crystals belong to the orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions, a = 85.6 A, b = 117.0 A, c = 1313.3 A
-
hanging-drop vapour-diffusion method, the crystals diffract to 2.0 A using synchrotron radiation, have unit-cell parameters a = 85.2, b = 118.0, c = 131.0 A, alpha = beta = gamma = 90 and show P2(1)2(1)2(1) symmetry
-
at 5C from a 30% saturated ammonium sulfate solution, yellow rod-shaped crystals
-
cocrystallization of ACO-II with lauroyl-CoA by the hanging-drop vapor-diffusion method under oil, to 2.07 A resolution
native ACO-II, hanging-drop vapor-diffusion method with 3% (w/v) polyethylene glycol 20000 as precipitant in 20 mM potassium phosphate, pH 7.4; X-ray structure analysis
-
to 2.74 A resolution by vapor diffusion hanging-drop method, unusual packing arrangement of the tomato AXC1 enzyme as compared to other ACX enzymes, three monomers of ACX1 are present in the asymmetric unit
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9
-
35C, 60 min
391050
6.5 - 7.5
Arthrobacter ureafaciens
at 37C
672429
7 - 9
-
stable for 120 min
674349
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 40
-
stable for 120 min
37.5 - 70
-
the ACOX1b isoform retains 57% of its specific activity at 50C and is more resistant to heat denaturation than ACOX1a since it conserves 30% of its specific activity after treatment at 50C, the isoform shows 70% specific activity at 37.5C
60
Arthrobacter nicotianae
-
30 min, with butyryl-CoA and FAD, 50% loss of activity; 30 min, with butyryl-CoA, without FAD, 85% loss of activity
65
-
10 min, complete inactivation
additional information
Arthrobacter nicotianae
-
FAD enhances thermal stability
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis, 4C, 24 h, 80% loss of activity
-
stabilization with benzoate necessary for purification of the holoenzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 25% glycerol, 8 months
-
-20C, for at least 1 month
-
-20C, pH 7.4, 2 months
-
-20C, potassium phosphate buffer, pH 7.0
Arthrobacter ureafaciens
-30C, 35% glycerol (v/v), at least 1 month
-
-30C, in presence of 35% v/v glycerol, stable for at least 1 year
-80C, wild-type enzyme and mutant enzymes E421D, E421A, E421Q and E421G are stable for 3 months
-
37C, 0.2 M potassium phosphate (pH 7.5) containing 0.1 M FAD, 4 h, less than 10% loss of activity
Arthrobacter ureafaciens
4C, His-tagged enzyme is stable for 1 week
-
4C, pH 7.4, 2 months, 20% loss of activity
-
frozen, 10% sucrose, several weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ACO-i and ACO-II, recombinant from Escherichia coli
-
both isoforms
-
by gel filtration and anion exchange chromatography
-
by gel filtration; Q-Sepharose column chromatography and CM-Sepharose column chromatography
Arthrobacter ureafaciens
holo- and apoenzyme
-
native and recombinant ACO-II from Escherichia coli
-
Ni-NTA column chromatography
-
nickel metal-affinity resin column chromatography
-
partially
recombinant from Escherichia coli
recombinant from Escherichia coli, His-tagged
-
recombinant His-tagged from Spodoptera frugiperda cells
-
to homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ACO-I and ACO-II; expression in Escherichia coli
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cloned into a bacterial expression vector pLM1 with six continous His codons attached to the 5' end of the gene, overexpression of wild-type ands mutant enzymes E421D, E421A, E421Q and E421G in Escherichia coli
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expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli JM109 cells; into vector pUTE300, expression in Escherichia coli JM109
Arthrobacter ureafaciens
expressed in Escherichia coli strains BL21 and C41, and in COS-7 cells (His-tagged enzyme)
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expression as His-tagged protein in Spodoptera frugiperda cells via infection with Baculovirus
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expression in COS-7 cells
expression in Escherichia coli
expression in Escherichia coli as an active, N-terminal tagged His6 fusion protein
expression in Escherichia coli BL 21
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expression in Escherichia coli of 2 genes: ACX1.1 and ACX1.2, sequence comparison with other species
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expression in Escherichia coli of His-tagged proteins: AtSACX, AtACX1, and AtACX3, sequence analysis also with AtACX2
expression of AtACX1 and AtACX2 in Escherichia coli; plant anti-sense constructs, investigation of substrate specificities and regulation
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expression of His-tagged enzyme in Escherichia coli
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expression of human ACOX1b isoform in a mouse ACOX1b mutant can reverse the null phenotype, overview
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gene aoxA, seuence comparisons, recombinant expression from plasmid in Aspergillus nidulans strain MH11036, complementation of enzyme deficient aoxADELTA strain MH11074, expression as GFP-tagged enzyme showing PexE-dependent peroxisomal localisation
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genes POX1-POX6, heterologous co-expression of the different isozymes with polyhydroxyalkanoate synthase (phaC) of Pseudomonas aeruginosa in Yarrowia lipolytica strains, subcloning in Escherichia coli
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His-tagged
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into the pET24 vector and transformed into Escherichia coli BL21(DE3)
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into vector pTZ18R
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into vector pUTE300, expression in Escherichia coli JM109
overexpression in Escherichia coli
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SCOX expression analysis in peroxisomal acyl-coenzyme A oxidase deficiency patients, overview
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sequence analysis
sequence analysis and regulation
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sequence analysis, expression analysis during development
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transformed SK32 cells stably expressing one of the wild type Pex5p isoforms, Pex5pM and S restore the processing of Aox, but Pex5pL does not
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C159T
Arthrobacter ureafaciens
60% activity compared to the wild type enzyme and shows increased sensitivity to N-ethylmaleimide; exhibits 60% activity of the wild-type enzyme, looses more than half of the activity after incubation with N-ethylmaleimide
C159T/C420S
Arthrobacter ureafaciens
activity less than one tenth of that of the wild type
C159T/C420S/C424V
Arthrobacter ureafaciens
shows no activity at all
C159T/C424V
Arthrobacter ureafaciens
activity less than one tenth of that of the wild type
C420S
Arthrobacter ureafaciens
41% activity compared to the wild type enzyme and shows increased sensitivity to N-ethylmaleimide; exhibits 41% activity of the wild-type enzyme, retains about 90% of the activity after incubation with N-ethylmaleimide
C420S/424V
Arthrobacter ureafaciens
activity less than one tenth of that of the wild type
C424V
Arthrobacter ureafaciens
98% activity compared to the wild type enzyme and shows increased sensitivity to N-ethylmaleimide; looses more than half of the activity after incubation with N-Ethylmaleimide
C159T
Arthrobacter ureafaciens NBRC 12140
-
60% activity compared to the wild type enzyme and shows increased sensitivity to N-ethylmaleimide; exhibits 60% activity of the wild-type enzyme, looses more than half of the activity after incubation with N-ethylmaleimide
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C420S
Arthrobacter ureafaciens NBRC 12140
-
41% activity compared to the wild type enzyme and shows increased sensitivity to N-ethylmaleimide; exhibits 41% activity of the wild-type enzyme, retains about 90% of the activity after incubation with N-ethylmaleimide
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C424V
Arthrobacter ureafaciens NBRC 12140
-
looses more than half of the activity after incubation with N-Ethylmaleimide
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G432R
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conversion of Aox from component A to components B and C is completely prevented at both 30C and 37C
G231V
the mutation in combination with skipping of exon 13 leads to peroxisomal acyl-CoA oxidase deficiency
R210H
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naturally occuring apparent homozygous missense mutation c.629G/A of SCOX in a peroxisomal acyl-coenzyme A oxidase deficiency patient
E421G
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inactive mutant enzyme
T138I
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compromised in wound-response signaling owing to a deficiency in jasmonic acid synthesis, FAD is not bound in the mutant protein
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
biotechnology
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potential depolluting agent by degradation of oils; several biotechnological applications: production of metabolites, such as citrate, secretion of proteins, degradation of fatty acids
degradation
medicine
nutrition
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engineering of plants with increased content of monocarboxylic fatty acids in this essential oil crop by enzyme overexpression
additional information
Show AA Sequence (200 entries)
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